Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding.

Journal Article

By using Tb3+ as a luminescent probe, we demonstrate that the phosphorylation state of a 14-residue peptide fragment of alpha-synuclein, a protein implicated in Parkinson's Disease, dramatically affects the metal ion affinity of the peptide. Whereas the unphosphorylated peptide and its phosphoserine analogue show weak Tb3+ binding, its phosphotyrosine analogue shows tight 1:1 binding as well as 2:1 and 3:1 Tb:peptide adducts. Our data suggest that the phosphorylated amino acid must be appropriately positioned among additional ligating residues to establish this phosphorylation-dependent metal binding.

Full Text

Duke Authors

Cited Authors

  • Liu, LL; Franz, KJ

Published Date

  • July 13, 2005

Published In

Volume / Issue

  • 127 / 27

Start / End Page

  • 9662 - 9663

PubMed ID

  • 15998051

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja043247v

Language

  • eng

Conference Location

  • United States